A flexible approach for understanding protein stability.
FEBS Lett
; 576(3): 468-76, 2004 Oct 22.
Article
en En
| MEDLINE
| ID: mdl-15498582
ABSTRACT
A distance constraint model (DCM) is presented that identifies flexible regions within protein structure consistent with specified thermodynamic condition. The DCM is based on a rigorous free energy decomposition scheme representing structure as fluctuating constraint topologies. Entropy non-additivity is problematic for naive decompositions, limiting the success of heat capacity predictions. The DCM resolves non-additivity by summing over independent entropic components determined by an efficient network-rigidity algorithm. A minimal 3-parameter DCM is demonstrated to accurately reproduce experimental heat capacity curves. Free energy landscapes and quantitative stability-flexibility relationships are obtained in terms of global flexibility. Several connections to experiment are made.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Conformación Proteica
/
Proteínas
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
FEBS Lett
Año:
2004
Tipo del documento:
Article
País de afiliación:
Estados Unidos